CPLM-006511

Genbank Nucleotide ID

Sterol O-acyltransferase 1

Protein Synonyms/Alias

Acyl-coenzyme A:cholesterol acyltransferase 1; ACAT-1; Cholesterol acyltransferase 1

ACACT; ACACT1; ACAT; ACAT1; SOAT; STAT

Homo sapiens (Human)

Position	Peptide	Type	References
45	SNGRIDIKQLIAKKI	ubiquitination	[1, 2, 3, 4]
120	RAPPEQGKIFIARRS	ubiquitination	[3, 5, 6, 7]
353	APLFRNIKQEPFSAR	ubiquitination	[3, 5]
531	ARQHCPLKNPTFLDY	ubiquitination	[1, 4]

[1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
[2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
[4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
[6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[7] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]

Functional Description

Catalyzes the formation of fatty acid-cholesterol esters. Plays a role in lipoprotein assembly and dietary cholesterol absorption. In addition to its acyltransferase activity, it may act as a ligase.

ACT_SITE 460 460 Potential.

Acyltransferase; Alternative splicing; Cholesterol metabolism; Complete proteome; Endoplasmic reticulum; Lipid metabolism; Membrane; Polymorphism; Reference proteome; Steroid metabolism; Sterol metabolism; Transferase; Transmembrane; Transmembrane helix.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005789; C:endoplasmic reticulum membrane; IDA:BHF-UCL.
GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
GO:0015485; F:cholesterol binding; IDA:BHF-UCL.
GO:0034736; F:cholesterol O-acyltransferase activity; IDA:BHF-UCL.
GO:0000062; F:fatty-acyl-CoA binding; IDA:BHF-UCL.
GO:0033344; P:cholesterol efflux; IMP:BHF-UCL.
GO:0034435; P:cholesterol esterification; IDA:BHF-UCL.
GO:0042632; P:cholesterol homeostasis; TAS:BHF-UCL.
GO:0008203; P:cholesterol metabolic process; IDA:BHF-UCL.
GO:0010878; P:cholesterol storage; IMP:BHF-UCL.
GO:0010742; P:macrophage derived foam cell differentiation; IMP:BHF-UCL.
GO:0042986; P:positive regulation of amyloid precursor protein biosynthetic process; IMP:BHF-UCL.
GO:0034379; P:very-low-density lipoprotein particle assembly; IMP:BHF-UCL.

IPR004299; MBOAT_fam.
IPR014371; Oat_ACAT_DAG_ARE.